Purification and characterization of cassiicolin, the toxin produced by Corynespora cassiicola, causal agent of the leaf fall disease of rubber tree

Cassiicolin, a phytotoxin produced by the necrotrophic fungus Corynespora cassiicola, was purified to homogeneity from a rubber tree isolate. The optimized protocol involves reverse phase chromatography followed by size exclusion chromatography, with monitoring of the toxicity on detached rubber tre...

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Bibliographic Details
Published in:Journal of chromatography. B, Analytical technologies in the biomedical and life sciences Analytical technologies in the biomedical and life sciences, 2007-04, Vol.849 (1), p.357-362
Main Authors: de Lamotte, Frédéric, Duviau, Marie-Pierre, Sanier, Christine, Thai, Robert, Poncet, Joël, Bieysse, Daniel, Breton, Frédéric, Pujade-Renaud, Valérie
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analysis
Analytical, structural and metabolic biochemistry
Ascomycota - metabolism
Biological and medical sciences
Cassiicolin
Chromatography
Chromatography, Liquid - methods
Corynespora cassiicola
Electrophoresis - methods
Fundamental and applied biological sciences. Psychology
General pharmacology
Hevea - drug effects
Hevea - microbiology
Hevea brasiliensis
Life Sciences
Mass spectrometry
Medical sciences
Molecular Sequence Data
Molecular Weight
Mycotoxins - chemistry
Mycotoxins - isolation & purification
Mycotoxins - toxicity
Pharmacology. Drug treatments
Plant Leaves - drug effects
Plant Leaves - microbiology
Purification
Reproducibility of Results
Sequence Analysis, Protein
Spectrometry, Mass, Electrospray Ionization - methods
Toxin
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Summary:Cassiicolin, a phytotoxin produced by the necrotrophic fungus Corynespora cassiicola, was purified to homogeneity from a rubber tree isolate. The optimized protocol involves reverse phase chromatography followed by size exclusion chromatography, with monitoring of the toxicity on detached rubber tree leaves. Cassiicolin appeared to be a peptide composed of 27 amino acids, glycosylated on the second residue, with a N-terminal pyroglutamic acid and 6 cysteines involved in disulfide bonds. Its molecular mass was estimated to be 2885 Da. No significant sequence homology with other proteins could be found. The availability of pure toxin in sufficient amount is a prerequisite for its structure determination, which is a key step in the understanding of the aggression mechanism.
ISSN:1570-0232
1873-376X
DOI:10.1016/j.jchromb.2006.10.051